Author : Maila E. Finch
Publisher :
Page : 172 pages
File Size : 23,57 MB
Release : 2005
Category : Metalloenzymes
ISBN :
Author : Michael K. Johnson
Publisher : John Wiley & Sons
Page : 941 pages
File Size : 31,86 MB
Release : 2017-08-14
Category : Science
ISBN : 1119159857
Summarizes the essential biosynthetic pathways for assembly of metal cofactor sites in functional metalloproteins Metalloprotein Active Site Assembly focuses on the processes that have evolved to orchestrate the assembly of metal cofactor sites in functional metalloproteins. It goes beyond the simple incorporation of single metal ions in a protein framework, and includes metal cluster assembly, metal-cofactor biosynthesis and insertion, and metal-based post-translational modifications of the protein environments that are necessary for function. Several examples of each of these areas have now been identified and studied; the current volume provides the current state-of-the-art understanding of the processes involved. An excellent companion to the earlier book in this series Metals in Cells—which discussed both the positive and negative effects of cellular interactions with metals—this comprehensive book provides a diverse sampling of what is known about metalloprotein active site assembly processes. It covers all major biological transition metal components (Mn, Fe, Co, Ni, Mo), as well as the other inorganic components, metal-binding organic cofactors (e.g., heme, siroheme, cobalamin, molybdopterin), and post-translationally modified metal binding sites that make up the patchwork of evolved biological catalytic sites. The book compares and contrasts the biosynthetic assembly of active sites involving all biological metals. This has never been done before since it is a relatively new, fast-developing area of research. Metalloprotein Active Site Assembly is an ideal text for practitioners of inorganic biochemistry who are studying the biosynthetic pathways and gene clusters involved in active site assembly, and for inorganic chemists who want to apply the concepts learned to potential synthetic pathways to active site mimics.
Author : Ivano Bertini
Publisher : CRC Press
Page : 1382 pages
File Size : 19,20 MB
Release : 2001-06-29
Category : Medical
ISBN : 9780824705206
This Handbook on Metalloproteins focuses on the available structural information of proteins and their metal ion coordination spheres. It centers on the metal ions indispensable for life but also considers metal ions used as substitution probes in studies of metalloproteins. Emphasizing the structure-function relationship, the book covers the common and distinct characterstics of metallo- enzymes, proteins, and amino acids bonded to copper, zinc, iron, and more.
Author : Albrecht Messerschmidt
Publisher : Wiley-Blackwell
Page : 816 pages
File Size : 35,36 MB
Release : 2001
Category : Science
ISBN :
The first two volumes of the "Handbook of Metalloproteins", published in 2001, focused on a number of metals, including iron, nickel, manganese, cobalt, copper and vanadium. Now we are delighted to present volume three which extends the wealth of knowledge and focuses on proteins found in the redox-inactive ions of zinc and calcium. (Midwest).
Author : H.A.O. Hill
Publisher : Springer Science & Business Media
Page : 222 pages
File Size : 43,21 MB
Release : 1999-04-01
Category : Science
ISBN : 9783540655534
Biological chemistry is a major frontier of inorganic chemistry. Three special volumes devoted to Metal Sites in Proteins and Models address the questions: how unusual ("entatic") are metal sites in metalloproteins and metalloenzymes compared to those in small coordination complexes? and if they are special, how do polypeptide chains and co-factors control this? The chapters deal with iron, with metal centres acting as Lewis acids, metals in phosphate enzymes, with vanadium, and with the wide variety of transition metal ions which act as redox centres. They illustrate in particular how the combined armoury of genetics and structure determination at the molecular level are providing unprecedented new tools for molecular engineering.
Author : Varrie Russell Smart
Publisher :
Page : 63 pages
File Size : 22,4 MB
Release : 2011
Category : Enzymes
ISBN :
Metalloenzymes make up approximately one third of all enzymes and catalyze a diverse range of reactions. Such enzymes include matrix metalloproteinases, carbonic anhydride, and the mononuclear non-heme iron(II) enzymes; all of which have been modeled using small molecular complexes to understand the structure and function. Symmetrical tripodal pseudopeptides were previously synthesized to model these enzymes, but they produced undesired complex polymers. Therefore, tert-butyl THB, a ligand with three tert-butyl histamines, was synthesized to produce a 1:1 metal/ligand binding mode. The tert-butyl THB ligand was confirmed by ESI-MS+ and NMR. In parallel, in order to accurately model more diverse active sites, such as those that contain two-histidines and one cysteine, two cysteines and one histidine, or two histidines and one carboxylate group, asymmetric ligands were synthesized which used the actual amino acid contained in the enzyme active site. These asymmetric ligands were partially synthesized and characterized, but require further development.
Author : Albrecht Messerschmidt
Publisher : Wiley
Page : 1500 pages
File Size : 44,13 MB
Release : 2001-08-16
Category : Science
ISBN : 9780471627432
"it is a pleasure just to read this handsome and carefully produced work" Angewandte Chemie 2002 "...the Handbook of Metalloproteins is highly recommended as a resource for bioinorganic chemistry. It will have lasting value for researchers in the field..." The Alchemist - Chemweb In recent years, the analysis and classification of metalloproteins at the interface between chemistry and biology has accelerated. Many developments and initiatives have taken place and this two-volume handbook provides a comprehensive, yet focussed, collection of 105 major metalloproteins. Content is presented in both a large format and full colour and covers the most relevant transition metals such as Iron, Nickel, Copper, Cobalt, Molybdenum, Manganese Tungsten and Vanadium. This is the first Handbook of Metalloproteins ever published and is comprised of articles written by renowned experts in the field. It draws together contributions from over two hundred internationally renowned researchers that include: Douglas Rees and Charles Stout as well as Nobel Prize winner Robert Huber. Each contribution is presented in a similar format and shows a ribbon plot of the overall 3D Structure on their first page, a representation of the metal active site and numerous other figures and tables underpinning the remarks. Comparative information is provided on different proteins and every entry has been extensively referenced to current literature. * First comprehensive handbook to cover the major metalloproteins * Presents structural and functional data in an organised manner * Incorporates full-colour representation of molecular structures throughout * Unifies information from molecular biology, enzymology, spectroscopy, biochemistry, chemistry, biophysics, macromolecular crystallography and structural biology * Includes comprehensive sections that cover: Functional Class, Occurrence, Amino Acid Sequence Information, Protein Production, Purification and Molecular Characterisation, Metal Content and Cofactors, Activity Test, Spectroscopy, 3D Structure, Functional Aspects.
Author : Bharat Kumar Sharma
Publisher :
Page : 145 pages
File Size : 38,14 MB
Release : 2016
Category :
ISBN :
Theoretical models and computational techniques are useful for gaining insight into the interactions, movements, and functions of atoms and molecules, ranging from small chemical systems with few atoms to large biological molecules with many atoms. Due to the inability of force field methods to accurately describe different properties of metalloenzymes and the prohibitive computing cost of high-level quantum methods, computationally efficient models are needed. This dissertation describes the development of new quantum semiempirical models for metalloproteins. The original AM1 (Austin Model 1) based on the neglect of diatomic differential overlap approximations was re-parameterized to describe the structural and energetic properties of biomolecules that mimic the active sites of metalloproteins. The biologically inspired genetic algorithm PIKAIA was used to optimize the parameters for each chemical element. Structures and energies of various clusters analogous to complexes found in metalloproteins were prepared as a training set using hybrid density functional theory. Models were trained to reproduce all of the properties included in the small training set. The optimized models were validated for large testing sets that incorporate bigger complexes and related reactions. Finally, the optimized models were used to study biologically-relevant processes in condensed phase using molecular dynamics simulations. All the gas- and liquid-phase results from the optimized models were compared with original semiempirical models as well as available high-level theoretical and experimental results. Metal ions play crucial roles in biological systems. They actively participate in structural, catalytic, and co-catalytic activities of a large number of enzymes. The development of semiempirical models is divided into three parts. First, new AM1 parameters for hydrogen and oxygen were developed to describe gas-phase proton transfer reactions in water and static and dynamic properties of liquid water. Gas-phase results were compared with original AM1, RM1, and PM3 models, whereas liquid results were compared with original AM1, AM1-W, and AM1PG-W models, and with available experimental results. It is found that the optimized model reproduces experimental data better than other available semiempirical models. Second, using the previously optimized model for hydrogen and oxygen, the AM1 model is re-parameterized for zinc and sulfur to describe important physical and chemical properties of zinc, water, hydrogen sulfide complexes mimicking structural motifs found in zinc enzymes. Metal-induced pKa shifts are computed for water and hydrogen sulfide, and compared with available theoretical and experimental results. Third, using previously optimized parameters for hydrogen, oxygen, and zinc, AM1 parameters for carbon and nitrogen are optimized to study proton transfer, nucleophilic attacks, and peptide hydrolysis mechanisms in zinc metalloproteases. Overall, the optimized models give promising results for the various properties of biomolecules in gas-phase clusters and in condensed phase. Particularly, the water model reproduces the proton transfer related properties in gas-phase and the structure, dielectric properties, and infrared spectra of liquid water. The zinc/sulfur model reproduces the hydration structure of zinc cation and zinc-bound hydrogen sulfide. Results for the coordination configurations of zinc solvated in water and in hydrogen sulfide confirm the versatility of the model. The optimized model for carbon and nitrogen improves the overall performance compared to AM1 and PM3. The optimized model for carbon and nitrogen reproduces structures and various energetic terms for zinc-ligands systems (representing the active sites of zinc enzymes) when compared to density functional theory results. The optimized model can be used to study metal-ligand reactivity in zinc enzymes.
Author : Curtis D. Klaassen
Publisher : Nelson Thornes
Page : 706 pages
File Size : 19,5 MB
Release : 1999
Category : Architecture
ISBN : 9783764358303
Metallothionein nomenclature and structure.- Nomenclature of metallothionein: Proposal for a revision.- Metallothionein: Molecular evolution and classification.- Structural and biological studies on native bovine Cu, Zn-metallothionein-3.- Circular dichroism, emission, and exafs studies of Ag(I), Cd(II), Cu(I), and Hg(II) binding to metallothioneins and modeling the metal binding site.- Metallothionein structure update.- Simulation of Zn/Cd binding in mammalian metallothionein domains.- The growth inhibitory activity of metallothionein-3 correlates with its novel ? domain sequence rather than metal binding properties.- Recombinant synthesis and metal-binding abilities of mouse metallothionein 1 and its ?- and ?-domains.- Biochemical characterization of monomeric and dimeric cadmium-substituted metallothionein-3.- Chemical and analytical aspects of metallothionein.- Mammalian metallothionein sub-isoform separation by RP-HPLC with on-line UV and electrochemical detection.- Characterisation of mammalian Cd, Zn metallothioneins using differential pulse polarography.- Comparison of CZE and MECC separations of MT isoforms.- Synthetic peptides and domains of metallothionein for structure function studies: rabbit liver peptide MT-IIA 49-61 and lobster MT ?N ?C and ?C?N domains.- Voltammetric methods in isolation and identification of plant metallothioneins from alga Chlorella.- Characterization of isometallothioneins in Chang liver cells and the transient accumulation of metallothionein and glutathione during cell proliferation.- Quantification of cytosolic metallothionein contents by a developed assay system using immobilized antibody.- Protein engineering of metallothionein to study on the metal-binding ability.- Metal binding proteins: Molecular engineering of improvements in metal specificity.- Molecular splicing of metallothionein - study on domains of metallothionein.- Metallothionein in non-mammalian tissues.- Involvement of metallothionein in female squirrelfish reproduction.- Accumulation of untranslated metallothionein mRNA in antarctic hemoglobinless fish (icefish).- Structure and function of metallothionein isoforms in terrestrial snails.- Functional and regulatory aspects of teleost metallothionein.- Metallothionein induction in mussels exposed to a metal mixture.- Synthesis and properties of class III metallothioneins of Schizosaccharomyces pombe in response to cadmium and zinc.- Phytochelatins (class III metallothioneins) and their desglycyl peptides induced by cadmium in root cultures of Rubia tinctorum L..- Chemical and spectroscopic properties of copper metallothionein from the copper resistant fungus Beauveria bassiana.- Transcription factors.- Metallothionein facts and frustrations.- Liver degeneration and embryonic lethality in mouse null mutants for the metal-responsive transcriptional activator MTF-1.- New insights into the mechanisms of cadmium regulation of mouse metallothionein-I gene expression.- Activation of mouse metallothionein I promoter by cadmium in human neuroblastoma cells.- Transcription factors involved in heavy metal regulation of the human metallothionein-IIA gene.- Transcriptional regulation of the gene encoding mouse metallothionein-3 and its expression in the organs of the reproductive system.- Dynamic regulation of yeast metallothionein gene transcription via metalloregulatory signaling factors.- Metal regulation of mammalian metal responsive element (MRE) binding proteins.- Metallothionein and hormone responsiveness.- Synergistic activation of mouse metallothionein-I gene by interleukin-6 and glucocorticoid.- Hammerhead ribozymes mediated down-regulation of rat metallothionein mrnas expression.- Inactivation of metal-induced metallothionein gene expression by protein kinase C inhibitor.- Cadmium-induced metallothionein expression and metallothionein mRNA in mice.- Role of metallothionein in reproduction, development and cell proliferation.- The nuclear-cytoplasmic presence of metallothion..
Author : Eugene Permyakov
Publisher : Wiley-Interscience
Page : 0 pages
File Size : 32,21 MB
Release : 2009-04-27
Category : Science
ISBN : 9780470392485
Synthesizes the current knowledge in the field and provides new insights into medical applications Metalloproteomics is the large-scale study of metal-binding proteins. These proteins, which represent about one quarter of all the proteins in the Protein Data Bank, play important roles in all biological systems and all biological processes. Metalloproteomics provides the latest information on all major families of metal-binding proteins, including their structural, physico-chemical, and functional properties, enabling readers to better understand these proteins. Moreover, the book demonstrates how understanding the structures, properties, and functions of intracellular and extracellular metal-binding proteins may unlock the key to drug development for the treatment of a myriad of diseases. Written by Eugene Permyakov, an international expert and pioneer in the structural analysis of metal-binding proteins, the book offers Theoretical introduction to cation binding Broad range of methods for investigating the binding of different cations to proteins Characteristics of interactions of physiologically important cations of Ca, Mg, Zn, Fe, Mn, Co, Cu, Ni, Mo, W, Na, and K with proteins Detailed considerations of structural and physico-chemical properties of the metal-binding proteins Interactions of all other metal cations with proteins Interactions of different types of cations with nucleic acids Throughout the text, the author integrates principles of proteomics. In addition, detailed examples underscore the role metal-binding proteins play in health and medicine. Bringing together and analyzing all the latest findings, Metalloproteomics' scope and level of insight are unparalleled. It is recommended for biophysicists, biochemists, enzymologists, cell and molecular biologists, protein and peptide scientists, organic and bioinorganic chemists, and chemical biologists.
